Hostname: page-component-cd9895bd7-dzt6s Total loading time: 0 Render date: 2024-12-27T10:28:57.653Z Has data issue: false hasContentIssue false
  • English
  • Français

Acute phase proteins in the domestic fowl

Published online by Cambridge University Press:  18 September 2007

R. Chamanza ,
L. van Veenm ,
M. T. Tivapasi  and
M. J. M. Toussaint
R. Chamanza
Affiliation:
Department of Pathology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508TD Utrecht, The Netherlands Department of Clinical Veterinary Studies, Faculty of Veterinary Science, University of Zimbabwe, P.O. Box MP 167, Mount Pleasant, Harare, Zimbabwe
L. van Veenm
Affiliation:
Poultry Health Section, Institute of Animal Health, Deventer, The Netherlands
M. T. Tivapasi
Affiliation:
Department of Pathology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508TD Utrecht, The Netherlands Department of Clinical Veterinary Studies, Faculty of Veterinary Science, University of Zimbabwe, P.O. Box MP 167, Mount Pleasant, Harare, Zimbabwe
M. J. M. Toussaint
Affiliation:
Department of Pathology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3508TD Utrecht, The Netherlands
Get access

Abstract

Post-mortem assessment of poultry health requires both identification and classification of the severity and chronicity of lesions. Such assessments are essential for deciding the necessity for treatment or its withdrawal. Poultry meat inspection and routine necropsies are also complicated by subclinical as well as hidden inflammatory processes which result in decreased production. Measurement of changes in the plasma levels of hepatic acute phase proteins in mammalian species is known to give an indication of the stage and severity of inflammatory processes as well as identifying inaccessible lesions. For poultry, several papers have been published on the plasma changes of some acute phase proteins in association with some common poultry diseases and general inflammatory processes. Some have corresponded well with the severity and stages of lesions. It is suggested that measurement of such proteins could be used to complement routine necropsy findings. Understanding the chicken acute phase response, major acute phase proteins present, and their advantages and shortfalls as markers of inflammation, is paramount to the achievement of these goals.

Keywords

Acute phase proteinschronicitydiagnosisdiseaseseveritylesionspoultry
Type
Research Article
Information
World's Poultry Science Journal , Volume 55 , Issue 1 , March 1999 , pp. 61 - 71
Copyright
Copyright © Cambridge University Press 1999

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Aisen, P. and Listowsky, I. (1980) Iron transport and storage proteins. Annual Review of Biochemistry 49: 357–393Google Scholar
Alsemgeest, S.M.P., Horagoda, A.Hulskamp-Koch, C.K., Tooten, P.C.J., Kim, D.H.Niewold, Th.A. and Gruys, E. (1995) First evidence for the existence of multiple isoforms of bovine serum amyloid-A (apoSAA). Scandinavian Journal of Immunology 41: 407–413Google Scholar
Amrani, D.L. (1990) Regulation of fibrinogen biosynthesis: glucocorticoid and interleukin 6 control. Blood Coagulation and Fibrinolysis 1: 443–446Google Scholar
Amrani, D.L.Mauzy-Melitz, D. and Mosesson, W.M. (1986) Effect of hepatocyte stimulating factor and glucocorticoids on fibronectin levels. Biochemistry Journal 238: 365–371Google Scholar
Bennett, M. and Schmid, K. (1980) Immunosuppression by human plasma α1-acid glycoprotein: importance of the carbohydrate moiety. Proceedings of the National Academy of Sciences of the USA 77: 6109–6113Google Scholar
Bories, P.N.Feger, J., Benbernou, N., Rouzeau, J.D.Agneray, J. and Durand, G. (1990) Prevalence of tri– and tetraantennary glycans of human α1-acid glycoprotein in release of macrophage inhibitor of interleukin–1 activity. Inflammation 14: 315–323Google Scholar
Bolin, C.A. (1986) Effects of exogenous iron on Escherichia coli septicemia in turkeys. American Journal of Veterinary Research 47: 1813–1816Google Scholar
Butlin, E.J.Curtis, M.J.Harry, E.G. and Deb, J.R. (1972) Effect of Escherichia coli endotoxins on plasma para-phenylenediamine oxidase (caeruloplasmin) activity in the domestic fowl. Journal of Comparative Pathology 82: 299–306Google Scholar
Butler, E.J. and Curtis, M.J. (1977) The effect of Escherichia coli endotoxin on plasma histaminase activity in the domestic fowl and the involvement of caeruloplasmin. Research in Veterinary Science 22: 267–270Google Scholar
Byrnes, S., Eaton, R. and Kogut, M. (1993) In vitro interleukin–1 and tumor necrosis factor alpha production by macrophages from chickens infected with either Eimeria maxima or Eimeria tenella. International Journal of Parasitology 23: 639–645Google Scholar
Charwood, P.A.Hatton, M.W.C., and Regoeczi, E. (1976) On the physiochemical and chemical properties of α,–acid glycoproteins from mammalian and avian plasmas. Biochemica et Biophysica Acta 453: 81–92Google Scholar
Curtis, M.J. and Butler, E.J. (1980) Response of ceruloplasmin to Escherichia coli endotoxin and adrenal hormones in the domestic fowl. Research in veterinary Science 28: 217–222Google Scholar
Curtis, M.J. and Thornton, G.A. (1973) The effect of heat killed Mycoplasma gallisepticum and M. meleagridis on plasma caeruloplasmin activity in the fowl. Research in Veterinary Science 15: 399–401Google Scholar
Curtis, M.J.Flack, I.H. and Harvey, S. (1980) The effects of Escherichia coli endotoxin on the concentration of corticosterone and growth hormone in the plasma of the domestic fowl. Research in Veterinary Science 28: 123–127Google Scholar
Damtew, B., Rzewnicki, D., Lozanski, G. and Kushner, L. (1993) IL-1 receptor antagonist affects the plasma protein response of Hep 3B cells to conditioned medium for lipopolysaccharide– stimulated monocytes. Journal of Immunology 150: 4001–4007CrossRefGoogle ScholarPubMed
Delers, F., Strecker, G. and Engler, R. (1988) Glycosylation of chicken haptoglobin: isolation and characterization of three molecular variants and studies of their distribution in hen plasma before and after turpentine-induced inflammation. Biochemistry and Cell Biology 66: 208–217Google Scholar
Dinarello, C.A. (1983) Pathogenesis of fever during hemodialysis. Contributions to Nephrology 36: 90–99Google Scholar
Dinarello, C.A. (1989) Interleukin–1 and its biological related cytokines. Advances in Immunology 44: 153–205Google Scholar
Grieninger, G., Liang, T.J.Beuving, G., Goldfarb, V., Metcalfe, S.A. and Muller-Eberhard, U. (1986) Hemopexin is a developmentally regulated, acute-phase plasma protein in the chicken. Journal of Biological Chemistry 261: 15719–15724Google Scholar
Grieninger, G., Oddoux, C., Diamond, L., Weissbach, L. and Plant, P.W. (1989) Regulation of fibrinogen synthesis and secretion by the chicken hepatocyte. Annals of the New York Academy of Sciences 557: 257–270CrossRefGoogle ScholarPubMed
Gruys, E. and Hol, P.R. (1984) Amyloid-A proteins in different species. Applied Pathology 2: 316–327Google Scholar
Gruys, E. and Landman, W.J.M. (1997) Acute phase proteins. Contribution for the European Davis Foundation Meeting, October 1997, Cheshire, UKGoogle Scholar
Gruys, E., Obwolo, M.J. and Toussaint, M.J.M. (1994) Diagnostic significance of the major acute phase proteins in veterinary clinical chemistry: a review. Veterinary Bulletin 64: 1009–1018Google Scholar
Hallquist, N.A. and Klasing, K.C. (1994) Serotransferrin, ovotransferrin and metallothionein levels during an immune response in chickens. Comparative biochemistry and physiology. Biochemistry and Molecular Biology 108: 375–384Google Scholar
Inoue, M.Satoh, W. and Mukarami, H. (1997) Plasma α1-acid glycoprotein in chickens infected with infectious bursa1 disease virus. Avian Diseases 41: 164–170Google Scholar
Itoh, H., Tamura, K., Izumi, M., Motoi, Y. and Funayama, Y (1993) Characterization of serum α1-acid glycoprotein in fetal and newborn calves during development. American Journal of Veterinary Research 54: 591–595Google Scholar
Iwamoto, M., Koike, T., Nakashima, K., Sato, K. and Kato, Y. (1989) Interleukin-1: a regulator of chondrocyte proliferation. Immunology Letters 21: 153–156Google Scholar
Johnson, R.W.Curtis, S.E.Dantzer, R., Bahr, J.M. and Kelley, K.W. (1993) Sickness behavior in birds caused by peripheral or central injection of endotoxin. Physiology and Behavior 53: 343–348Google Scholar
Kaplan, S.S.Quie, P.G. and Basford, R.E. (1975) Effect of iron on leukocyte function: inactivation of H2O2 by iron. Infection and Immunity 12: 303–308CrossRefGoogle ScholarPubMed
Kent, J. (1992) Acute phase proteins: their use in veterinary diagnostics. British Veterinary Journal 148: 279–282Google Scholar
Kimura, M., Toth, L. A., Agostini, H.Cady, A.B.Majde, J.A. and Krueger, J. M (1995) Comparison of acute phase responses induced in rabbits by lipopolysaccharide and doublestranded RNA. American Journal of Physiology 267: R1596–R1605Google Scholar
Klasing, K.C. (1984) Effect of inflammatory agents and interleukin 1 on iron and zinc metabolism. American Journal of Physiology 247: R901–R904Google Scholar
Klasing, K.C. (1994) Avian leukocytic cytokines. Poultry Science 73: 1035–1043CrossRefGoogle ScholarPubMed
Klasing, K.C. and Barnes, D.M. (1988) Decreased amino acid requirements of growing chicks due to immunological stress. Journal of Nutrition 118: 1158–1164Google Scholar
Klasing, K.C. and Johnstone, B.C. (1991) Monokines in growth and development. Poultry Science 70: 1781–1789Google Scholar
Klasing, K.C. and Korver, D.R. (1997) Leukocytic cytokines regulate growth rate and composition following activation of the immune system. Journal of Animal Science 75 (Supplement 2): 58–67Google Scholar
Klasing, K.C. and Peng, R.K. (1987) Influence of cell sources, stimulating agents and incubating conditions on release of interleukin–1 from chicken macrophages. Developmental and Comparative Immunology 2: 385–394CrossRefGoogle Scholar
Klasing, K.C. and Peng, R.K. (1990) Monokine–like activities released from a chicken macrophage line. Animal Biotechnology 1: 107–120Google Scholar
Klasing, K.C.Laurin, D.E.Peng, R.K. and Fry, D.M. (1987) Immunologically mediated growth depression in chicks: influence of feed intake, corticosterone and interleukin-1. Journal of Nutrition 117: 1629–1637Google Scholar
Koh, T.S.Peng, R.K. and Klasing, K.C. (1996) Dietary copper level affects copper metabolism during lipopolysaccharide-induced immunological stress in chicks. Poultry Science 75: 867–872Google Scholar
Koj, A. (1985) Definition and classification of acute-phase proteins. In: The Acute Phase Response to Injury and Infection(Eds Gordon, A.H. and Koj, A.), Elsevier, Amsterdam, pp. 139–145Google Scholar
Korver, D.R. and Klasing, K.C. (1997) Dietary fish oil alters specific and inflammatory immune responses in chicks. Journal of Nutrition 127: 2039–2046Google Scholar
Kuhlman, M., Joiner, K.A. and Ezekowitz, R.A.B. (1989) The human mannose-binding protein functions as an opsonin. Journal of Experimental Medicine 189: 1733–1745CrossRefGoogle Scholar
Landman, W.J.M., Gruys, E. and Dwars, R.M. (1994) A syndrome associated with growth depression and amyloid arthropathy in layers: a preliminary report. Avian Pathology 23: 461–470CrossRefGoogle ScholarPubMed
Landman, W.J.M., Sletten, K., Koch, C.A.M., Tooten, P.C.J. and Gruys, E. (1996) Chicken amyloid protein is of AA-type. Characterization of chicken amyloid protein. Scandinavian Journal of Immunology 43: 210–218Google Scholar
Laudert, E. and Harrington, S. (1994) Use of acute phase proteins as indicators of inflammation in domestic poultry. Proceedings of the 43rd Western Poultry Disease ConferenceSacramento, CaliforniaGoogle Scholar
Ling, Y.S.Mao, H.P.Zhong, A.C. and Guo, Y.C. (1991) The effects of Escherichia coli and its endotoxin on amyloidogenesis in ducks. Veterinary Pathology 28: 519–523Google Scholar
Luthman, J., Jacobsson, S.O. and Frank, A. (1991) Endotoxin-induced changes in plasma mineral and vitamin levels in calves. Acta Veterinaria Scandinavica 32: 403–404Google Scholar
Musquera, S., Lombart, C.Jayle, M.F.Rogard, M. and Walks, M. (1979) Identification of haptoglobin in chickens serum and specificity of the chicken haptoglobin-hemoglobin complex formation. Comparative Biochemistry and Physiology 62: 242–244Google Scholar
Nair, M.K. (1973) The early inflammatory reaction in the fowl. Acta Veterinaria Scandinavica Supplement 42: 1–103Google Scholar
Nakamura, K., Imai, K. and Tanimura, N. (1996) Comparison of the effects of infectious bronchitis and infectious laryngotracheitis on the chicken respiratory tract. Journal of Comparative Pathology 114: 11–21CrossRefGoogle ScholarPubMed
Nakamura, K., Mase, M., Tanimura, N., Yamaguchi, S., Nakazawa, M., and Yuasi, N. (1997) Swollen head syndrome in broiler chickens in Japan: its pathology, microbiology and biochemistry. Avian Pathology 26: 139–154Google Scholar
Nimmer, D., Bergtrom, G., Hirano, H. and Amrani, D.L. (1987) Regulation of plasma fibronectin biosynthesis by glucocorticoids in chick hepatocyte cultures. Journal of Biological Chemistry 262: 10369–10375CrossRefGoogle ScholarPubMed
Patterson, L.T. and Mora, E.C. (1965) Occurrence of a substance analogous to C-reactive protein in the blood of the domestic fowl. Texas Reports on Biology and Medicine 22: 716–721Google Scholar
Pepys, M.B. and Baltz, M.L. (1983) Acute phase proteins with special reference to C-reactive protein and related proteins (pentraxins) and serum amyloid-A protein. Advances in Immunology 34: 141–212Google Scholar
Pepys, M.B.Baltz, M.L., Tennent, G.A.Kent, J., Ousey, J. and Rossdale, P.D. (1989) Serum amyloid-A (SAA) in horses: objective measurement of the acute-phase response. Equine Veterinary Journal 21: 106–109Google Scholar
Piercy, D.W .T. (1979) Acute phase responses to experimental salmonellosis in calves and colibacillosis in chickens: serum iron and ceruloplasmin. Journal of Comparative Pathology 89: 309–319.CrossRefGoogle Scholar
Richard, M.P. and Augustine, P.C. (1988) Serum and liver zinc, copper and iron in chicks infected with Eimeria aceroulina or Eimeria tenella. Biologiral Trace Element Research 17: 207–219Google Scholar
Samad, F., Bergtrom, G., Eissa, H. and Amrani, D.L. (1993) Stimulation of chick hepatocyte fibronectin production by fibroblasts-conditioned medium is due to interleukin 6. Biochemica et Biophysica Acta 1181: 207–213Google Scholar
Saini, P.K. and Webert, D.W. (1991) Application of acute phase reactants during antemortem and postmortem meat inspection. Journal of the American verterinary Medical Association 198: 1898–1902.Google Scholar
Schat, K.A. and Kaiser, P. (1997) Avian cytokines. In: Cytokines in Verterniary Medicine (Schijns, V.E.C.J. and Horzineck, M.C. Eds), CAB International, pp. 289–297Google Scholar
Schonsinky, K. (1974) Measurement of cerulopbsniin from oxidase activity in serum by use of o-diansidine hydrochloride. Clinical Chemistry 20: 1556–1563Google Scholar
Sehgal, P.B.Grieninger, G. and Tosato, G. (Eds)(1989) Regulation of the acute phase and the immune responses: interleukin 6. Anuals of the New York Academy of Sciences 557: 1–580Google Scholar
Singh, G. (1988) Electrophoretic study of laying hens serum by crossed imununoelectrophoresis. Acta Veterinaria Hungarian 36: 209–211Google Scholar
Sugii, S. and Hirota, Y. (1993) A Ca2 –dependent phosphorylcholine-binding protein in chicken serum. Journal of Veterniary Medical Science 55: 841–843Google Scholar
Sugii, S. and Hirota, Y. (1994) Identification and carbohydrate specificity of a chicken serum mannan-binding protein reactive with a Ra chemotype strain of Salmonella typhimurium. Journal of Veterinary Medical Science 56: 747–751Google Scholar
Takahashi, K., Kaji, N., Akiba, Y. and Tamura, K. (1994) Plasma alpha acid glycoprotein concentration in broilers: Influence of age, sex and injection of Escherichia coli lipopolysaccharide. British Poultry Science 35: 427–432Google Scholar
Takahashi, K., Ohta, N. and Akiba, Y. (1997) Influence of dietary methionine and cysteine on metabolic responses to immunological stress by Escherichia coli lipopolysaccharide injection, and mitogen response in broilers. British Journal of Nutrition 78: 815–821CrossRefGoogle Scholar
Takahashi, K., Yodogawa, S. and Akiba, Y (1995) Effect of dietary protein concentration on responses to Escherichia coli endotoxin in broiler chickens. British Journal of Nutrition 74: 173–182Google Scholar
Tohjo, H., Miyoshi, F., Uchida, E., Niyama, M., Syuto, B., Moritsu, Y., Ichikawa, S. and Takeuchi, M. (1995) Polyacrylamide gel electrophoretic patterns of chicken serum in acute inflammation induced by intramuscular injection of turpentine. Poultry Science 74: 648–655Google Scholar
Tohjo, H., Yadatsu, M., Uchida, E., Niyama, M., Syuto, B., Moritsu, Y., Ichikawa, S. and Takeuchi, M. (1996) Polyacrylamide gel electrophoretic serum protein patterns of acute inflammation induced by intramuscular injection of turpentine in young broiler chickens. Journal of Veterinary Medical Science 58: 267–268CrossRefGoogle ScholarPubMed
Torres-Medina, A., Mussman, H.C.Rhodes, M.B. and Twiehaus, M.J. (1973) Chicken transferrin: high levels in chicken with reticuloendothelial virus disease. Poultry Science 52: 747–754CrossRefGoogle ScholarPubMed
Toussaint, M.J.M., Van Ederen, A.M. and Gruys, E. (1995) Implications of clinical pathology in assessment of animal health and in animal production and meat inspection. Comparative Hematology International 5: 149–157Google Scholar